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Label-free protein quantification in freshly ejaculated versus post-mating spermatophores of the noble crayfish Astacus astacus.

  • Hamid Niksirat
  • Peter James
  • Liselotte Andersson
  • Antonín Kouba
  • Pavel Kozák
Publishing year: 2015
Language: English
Pages: 70-77
Publication/Series: Journal of Proteomics2008-01-01+01:00
Volume: 123
Document type: Journal article
Publisher: Elsevier

Abstract english

Crayfish spermatophores are deposited on the body surface of the female during mating and remain there for a period of time before fertilization ensues. Post-mating changes in protein expression level in the noble crayfish Astacus astacus spermatophore were quantified. In-gel digestion and high resolution mass spectrometry were used for label-free protein quantification. One hundred twelve proteins were identified in the spermatophore of noble crayfish. After 7days of storage on the body of the female, 6 proteins were identified in the post-mating spermatophore that showed significant up-regulation and 4 significant down-regulations (p<0.05, fold change ≥2). The highest rate of up-regulation was observed in sodium/hydrogen exchanger, which may indicate the importance of intracellular pH adjustment for final maturation of the crayfish spermatozoon. The highest rate of down-regulation was observed in histone H2A. This may increase chromatin flexibility and facilitate its transfer into the oocyte during fertilization. The vitellogenin protein was identified in the crayfish spermatophore and its level changed during storage on the body surface of female. Extensive proteomic modification of male gametes during storage on the body surface of the female suggests post-mating final maturation of the crayfish spermatozoon.


  • Immunology in the medical area


  • ISSN: 1874-3919
Peter James
E-mail: peter [dot] james [at] immun [dot] lth [dot] se


Department of Immunotechnology

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